Skip to Content
Merck
All Photos(1)

Documents

SRP5256

Sigma-Aldrich

HSP90β, His tagged human

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

D6S182, HSP90AB1, HSP90B, HSPC2, HSPCB

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

Assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

~91 kDa

NCBI accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HSP90AB1(3326)

General description

HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins. HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis.

Biochem/physiol Actions

Heat shock protein 90kDa α family class B member 1 (HSP90AB1) is expressed in cancers and has a role in the infection of Japanese encephalitis virus. It also takes part in signal transduction pathways.

Physical form

Supplied in 50 mM sodium phosphate, pH 7.0, 300 mM NaCl, 150 mM imidazole, 0.1 mM PMSF, 0.2 mM DTT, 25% glycerol.

Preparation Note

After opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Heat-shock protein 90 inhibitors in cancer therapy: 17AAG and beyond.
Georgakis GV and Younes A
Future Oncology, 1(2), 273-281 (2005)
Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
Bin Chen
BMC Genomics, 7, 156-156 (2006)
Yueh-Liang Tsou et al.
PloS one, 8(10), e77133-e77133 (2013-10-08)
Although several factors participating in enterovirus 71 (EV71) entry and replication had been reported, the precise mechanisms associated with these events are far from clear. In the present study, we showed that heat shock protein 90 (HSP90) is a key
Yan Zhao et al.
PloS one, 8(3), e58646-e58646 (2013-03-22)
Variations in genetic background are the leading cause of differential susceptibility to traumatic infection. Heat shock protein 90 (HSP90), a broadly distributed and conserved molecule, regulates inflammation under stressful and traumatic conditions. However, the relationships between HSP90 genetic polymorphisms, post-traumatic
Morgan C Hunter et al.
PloS one, 9(1), e86842-e86842 (2014-01-28)
Heat shock protein 90 (Hsp90) has been identified in the extracellular space and has been shown to chaperone a finite number of extracellular proteins involved in cell migration and invasion. We used chemical cross-linking and immunoprecipitation followed by tandem mass

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service